Goat anti rabbit igg

Manufactured by GeneTex

Sourced in United States

Goat anti-rabbit IgG is a secondary antibody that binds to rabbit primary antibodies. It is used to detect and visualize rabbit antibodies in various immunoassays and techniques.

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Lab products found in correlation

Rabbit anti mouse igg, by GeneTex (4 mentions) Flotillin 2, by MDBio (2 mentions) Flotillin 2, by Santa Cruz Biotechnology (2 mentions) Anti n cadherin, by GeneTex (1 mentions) Anti e cadherin, by GeneTex (1 mentions) Anti fibronectin, by GeneTex (1 mentions) Western blotting detection kit, by Solarbio (1 mentions) Pvdf membrane, by Merck Group (1 mentions) Ripa lysis buffer, by Beyotime (1 mentions) Anti gapdh, by GeneTex (1 mentions) Ecl reagent, by Merck Group (1 mentions) E cadherin antibody, by Cell Signaling Technology (1 mentions) Goat anti mouse igg, by GeneTex (1 mentions) Biospectrum 600 imaging system, by Analytik Jena (1 mentions) Glial fibrillary acidic protein (gfap), by Thermo Fisher Scientific (1 mentions) Calnexin h 70, by Santa Cruz Biotechnology (1 mentions) Ponceau s stain, by Merck Group (1 mentions) Animage quant las4000, by GE Healthcare (1 mentions) Tsg101 c 2, by Santa Cruz Biotechnology (1 mentions) Cd81 h 121, by Santa Cruz Biotechnology (1 mentions)

5 protocols using goat anti rabbit igg

Antibody Characterization for Gill Proteins

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The primary antibodies used in this study included (i) a mouse monoclonal antibody (α5, DHSB, Iowa City, IA, USA) raised against the avian NKA α-subunit (Lin et al., 2003; Yang et al., 2015) , (ii) a mouse monoclonal antibody (flotillin-2, Santa Cruz, CA, USA) raised against the amino acids 150-240 of human flotillin-2 (XP_016879883.1) with approximately 83% similarity with milkfish flotillin-2 (XP_030648347.1) and 80% similarity with tilapia flotillin-2 (XP_003456181.1), and (iii) a rabbit polyclonal antibody (MDBio, Taipei, Taiwan) raised against the specific epitope (AEMPADSGYPAYLGARLA) of the pufferfish (Tetraodon nigroviridis) VHA A (ABX80240.1) with 100 % similarity with milkfish VHA A isoform1 and isoform 2, as well as tilapia VHA A (BAF94024.1). The sequences of two isoforms of VHA A found in the milkfish transcriptome database (Hu et al., 2015) were showed in Fig. S1. The specificities of the VHA A antibody to gills of tilapia and milkfish were tested and showed in Fig. S2. According to the primary antibodies, the secondary antibodies for immunoblots included the horseradish peroxidase-conjugated (i) rabbit anti-mouse IgG, (ii) goat anti-rabbit IgG, and (iii) rabbit anti-goat IgG (GeneTex, Irvine, CA, USA). The similarity between flotillin-2 with milkfish.

Lin Y.T., Hu Y.C., Wang Y.C., Hsiao M.Y., Lorin-Nebel C, & Lee T.H. (2021). Differential expression of two ATPases revealed by lipid raft isolation from gills of euryhaline teleosts with different salinity preferences. Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology, 253.

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Western Blotting of Epithelial Markers

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Proteins were isolated using radioimmunoprecipitation assay (RIPA) lysis buffer (Beyotime). Protein samples (30 μg) were segregated by SDS‐PAGE gel and transferred onto polyvinylidene difluoride (PVDF) membranes (Millipore). The membranes were blocked in skim milk, and then incubated with primary antibodies: anti‐E‐cadherin (1:5000, GeneTex), anti‐N‐cadherin (1:3000, GeneTex), anti‐fibronectin (1:3000, GeneTex), anti‐XRCC5 (1:2000, Solarbio) or anti‐GAPDH (1:10000, GeneTex). Then, the membranes were reacted with secondary antibody (Goat Anti‐Rabbit IgG, 1:50000, GeneTex). Finally, protein bands were examined using a western blotting detection kit (Solarbio).

Ayoufu A., Paierhati P., Qiao L., Zhang N, & Abudukeremu M. (2023). RUSC1‐AS1 promotes the malignant progression of breast cancer depending on the regulation of the miR‐326/XRCC5 pathway. Thoracic Cancer, 14(24), 2504-2514.

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Western Blot Analysis of EBV Proteins

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Cell lysates were prepared, quantified and immobilized on PDVF membranes as described previously. The membranes were incubated with a rabbit monoclonal anti-CDH1 (E-cadherin) antibody (1∶5000; Cell signaling #4065), anti-LMP1 monoclonal antibody (S12) (1∶1000; a gift from Dr. Yu-Sun Chang, Chang Gung University), rat monoclonal anti-LMP2A antibody (1∶1000; Bio-Rad MCA2466), anti-EBNA1 antibody (1∶1000; a gift from Dr. Mei-Ru Chen, National Taiwan University) followed by horseradish peroxidase-conjugated goat anti-rabbit IgG or goat anti-mouse IgG (1∶10000; GeneTex #213110-01, #213111-01) and the resultant bands were detected using ECL reagents (Millipore). An anti-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) antibody (1∶10000; BioWorld) was employed as a loading control. Western blot images were captured with the UVP BioSpectrum 600 Imaging System (Upland, CA, USA), and the band intensity was quantified with the Image J software.

Hsu C.Y., Yi Y.H., Chang K.P., Chang Y.S., Chen S.J, & Chen H.C. (2014). The Epstein-Barr Virus-Encoded MicroRNA MiR-BART9 Promotes Tumor Metastasis by Targeting E-Cadherin in Nasopharyngeal Carcinoma. PLoS Pathogens, 10(2), e1003974.

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Western Blot Analysis of Extracellular Vesicles

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Whole-cell lysates were prepared by washing cells with PBS, pelleting, then lysing with radioimmunoprecipitation assay (RIPA) buffer as described previously 6 (link). Equal protein of cell lysates and EV samples were measured by Pierce 660 nm Protein Assay (Invitrogen, 22,662) then loaded into an SDS 10% or 12% polyacrylamide gel. Western blot analysis was performed as described 57 . Ponceau S stain (Sigma, P7170) was used to visualize total protein. Blots were probed with the following antibodies: TSG101 (4A10; Genetex), CD63 (TS63; Abcam), CD9 (MM2/57; Millipore), Syntenin-1 (S-31; Santa Cruz), Calnexin (H-70; Santa Cruz), Aβ (2454; Cell Signaling), GFAP (PA5-16291, ThermoFisher), rabbit anti-mouse IgG (Genetex, GTX213112-01), goat anti-rabbit IgG (Genetex, GTX213110-01). Blots were imaged using a Bio-Rad ChemiDoc imager and processed using ImageQuant TL v8.1.0.0 software and CorelDraw Graphic Suite X5.

Cone A.S., Yuan X., Sun L., Duke L.C., Vreones M.P., Carrier A.N., Kenyon S.M., Carver S.R., Benthem S.D., Stimmell A.C., Moseley S.C., Hike D., Grant S.C., Wilber A.A., Olcese J.M, & Meckes DG J.r. (2021). Mesenchymal stem cell-derived extracellular vesicles ameliorate Alzheimer's disease-like phenotypes in a preclinical mouse model. Theranostics, 11(17), 8129-8142.

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Isolation and Analysis of Extracellular Vesicles

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To prepare brain homogenates, tissue was removed from the frontal lobe,
lysed in strong lysis buffer (detailed above) with proteinase inhibitor,
homogenized by pipette, and centrifuged at 10,000 × g for 10 minutes to
discard whole cells and intact cellular debris. For confirmation of EV proteins
in purified lysates, 5X Laemmli sample buffer [10% SDS, 250 mM Tris pH 6.8, 1
mg/mL bromophenol blue, 0.5 M DTT, 50% glycerol, 5% BME] was added to EV
isolates for a final concentration of 1X. For immunoblot analysis of CD63, DTT
and BME were omitted from lysis and sample buffers to allow the protein to run
in non-reducing conditions. Gel electrophoresis and western blotting was
performed as previously described (Hurwitz et
al., 2017b). Equal volume of gradient lysates were loaded into an
SDS-PAGE gel. Blots were probed with the following antibodies: Alix (Q-19; Santa
Cruz Biotechnology), HSC70 (B-6; Santa Cruz), TSG101 (C-2; Santa Cruz), CD63
(TS63; Abcam), Rab8a (63-BJ ; Santa Cruz), and CD81 (H-121 ;Santa Cruz), rabbit
anti-mouse IgG (Genetex, 26728), rabbit anti-goat IgG (Genetex, 26741), goat
anti-rabbit IgG (Fab fragment) (Genetex, 27171). Blots were imaged using an
Image Quant LAS4000 (General Electric) and processed with ImageQuant TL v8.1.0.0
software, Adobe Photoshop CS6 and CorelDraw Graphic Suite X5.

Hurwitz S.N., Sun L., Cole K.Y., Ford CR I.I.I., Olcese J.M, & Meckes DG J.r. (2018). An optimized method for purification of whole brain-derived extracellular vesicles reveals insight into neurodegenerative processes in a mouse model of Alzheimer’s disease.. Journal of neuroscience methods, 307, 210-220.

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